GenomeNet

Database: UniProt
Entry: G0AJC7_COLFT
LinkDB: G0AJC7_COLFT
Original site: G0AJC7_COLFT 
ID   G0AJC7_COLFT            Unreviewed;       388 AA.
AC   G0AJC7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Putative NOL1/NOP2/sun family protein {ECO:0000313|EMBL:AEK61061.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:AEK61061.1};
GN   OrderedLocusNames=CFU_1229 {ECO:0000313|EMBL:AEK61061.1};
OS   Collimonas fungivorans (strain Ter331).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=1005048 {ECO:0000313|EMBL:AEK61061.1, ECO:0000313|Proteomes:UP000008392};
RN   [1] {ECO:0000313|EMBL:AEK61061.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK61061.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=15305924; DOI=10.1111/j.1462-2920.2004.00673.x;
RA   Leveau J.H., Gerards S., de Boer W., van Veen J.A.;
RT   "Phylogeny-function analysis of (meta)genomic libraries: screening for
RT   expression of ribosomal RNA genes by large-insert library fluorescent in
RT   situ hybridization (LIL-FISH).";
RL   Environ. Microbiol. 6:990-998(2004).
RN   [2] {ECO:0000313|EMBL:AEK61061.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK61061.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=16457898; DOI=10.1016/j.mimet.2005.12.010;
RA   Leveau J.H., Gerards S., Fritsche K., Zondag G., van Veen J.A.;
RT   "Genomic flank-sequencing of plasposon insertion sites for rapid
RT   identification of functional genes.";
RL   J. Microbiol. Methods 66:276-285(2006).
RN   [3] {ECO:0000313|EMBL:AEK61061.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK61061.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=18671744; DOI=10.1111/j.1574-6941.2008.00547.x;
RA   Fritsche K., de Boer W., Gerards S., van den Berg M., van Veen J.A.,
RA   Leveau J.H.;
RT   "Identification and characterization of genes underlying chitinolysis in
RT   Collimonas fungivorans Ter331.";
RL   FEMS Microbiol. Ecol. 66:123-135(2008).
RN   [4] {ECO:0000313|EMBL:AEK61061.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK61061.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=19638176; DOI=10.1111/j.1462-2920.2009.02010.x;
RA   Leveau J.H., Uroz S., de Boer W.;
RT   "The bacterial genus Collimonas: mycophagy, weathering and other adaptive
RT   solutions to life in oligotrophic soil environments.";
RL   Environ. Microbiol. 12:281-292(2010).
RN   [5] {ECO:0000313|EMBL:AEK61061.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK61061.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=21614084; DOI=10.1038/ismej.2011.29;
RA   Mela F., Fritsche K., de Boer W., van Veen J.A., de Graaff L.H.,
RA   van den Berg M., Leveau J.H.;
RT   "Dual transcriptional profiling of a bacterial/fungal confrontation:
RT   Collimonas fungivorans versus Aspergillus niger.";
RL   ISME J. 5:1494-1504(2011).
RN   [6] {ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|Proteomes:UP000008392};
RA   Leveau J.H.;
RT   "Complete sequence of Collimonas fungivorans Ter331.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002745; AEK61061.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0AJC7; -.
DR   STRING; 1005048.CFU_1229; -.
DR   KEGG; cfu:CFU_1229; -.
DR   eggNOG; COG0144; Bacteria.
DR   HOGENOM; CLU_005316_0_2_4; -.
DR   Proteomes; UP000008392; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22807:SF77; SUN PROTEIN; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000008392};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}.
FT   DOMAIN          95..372
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        309
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         209
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         256
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   388 AA;  42252 MW;  C3A80704986E9101 CRC64;
     MVAEAVYGLL RNKAIYTSFA ESGNGPTMRR MTLLGLADAV SIESLGGLSD EEIEWLKRVA
     EIDRNLMPPL MRSNLPQWLF DKLVARDGEA ATLQLAHAMN QPAPLDLRVN SLKANREEVI
     TALAEAPILC EPTPYAPLGL RVIKKPTLQN LPLFKSGAIE VQDEGSQLLA QIVGAKRGEM
     VVDFCAGAGG KTLALGATMR NTGRLYAFDV SEKRLAKLKP RMARSGLSNI HPVLIAHEND
     GKVKRLAGKI DRVLVDAPCS GLGTLRRNPD VKWRQTPEAI AEMNVKQIAI LSSAARLVKS
     GGRLVYGTCS LLDEENDAIA AQFLASHEDF SLLPMKDVLA EQKIELEMGD YLKLLPHQHQ
     TDGFFAAVFV RKAAGGSADK EKREDVAP
//
DBGET integrated database retrieval system